ID Q8NNM9_CORGL Unreviewed; 651 AA.
AC Q8NNM9; Q6M3R8;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Cell division protein FtsI/penicillin-binding protein 2 {ECO:0000313|EMBL:BAB99557.1};
GN OrderedLocusNames=Cgl2164 {ECO:0000313|EMBL:BAB99557.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB99557.1, ECO:0000313|Proteomes:UP000000582};
RN [1] {ECO:0000313|Proteomes:UP000000582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; BA000036; BAB99557.1; -; Genomic_DNA.
DR RefSeq; NP_601366.1; NC_003450.3.
DR RefSeq; WP_011014926.1; NC_006958.1.
DR AlphaFoldDB; Q8NNM9; -.
DR STRING; 196627.cg2375; -.
DR KEGG; cgl:Cgl2164; -.
DR PATRIC; fig|196627.13.peg.2102; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_5_11; -.
DR OrthoDB; 9789078at2; -.
DR BioCyc; CORYNE:G18NG-11756-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:BAB99557.1};
KW Cell division {ECO:0000313|EMBL:BAB99557.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000582};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..232
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 310..628
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 651 AA; 69770 MW; B02EE3ED672DAB14 CRC64;
MTYRPKSSTQ GGARKRRVNM VTAIALVIAG VLIIRLGWVQ VVWGPELSLN ASEQRTRVYV
DPARRGSIVD REGNQMAYTM QARSLTVSPN IMREELKTGT DLALRLAAEE TDPENVASYV
TIEEGNAYVF ASEEQRETIL SDKVEERIQS IADRIPEIIK SHDQDVTGIS SEEILDKLNA
DSQYEVLVRN VDPDVASEIT DEMPSVAADH QDIRQYPNGA IGENIIGRIS MDGEGQFGFE
ASNDSLLAGN NGRSTQDMSI LGQAIPGTLR DQIPAIDGAS VELTVDLDLQ TYVQQALEQA
KANSGAENAS AVVLDAKTAE VLAMANTDTI NPNEDTGKQI EQGKSFDNPS VTHPFEPGSV
AKVITAAGVI QEGLTTPDEV LQVPGSIEMA GVSVGDAWDH GVVPYTTAGI FGKSSNVGTL
MLAQRLGEDK FADYLERFGV GQPTGIELPS ESQGLLPARE QWSGGTFANL PIGQGMSITT
LQMAGIYQAL ANDGERIQPR IIKSVTDSDG TVLEQPEPDK IQVVSAEAAR TTVDMFRSVT
QVDPTGVQQG TAPDASIEGY QISGKTGTAQ KVDPNTGAYS NSQYWITFAG IAPADDPRFV
VAIMLDEPER GVHGGGGQTA APLFKDIATW LLNRDNIPLS AATEPIILQA Q
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